Structure of PDB 6zn2 Chain E Binding Site BS03

Receptor Information
>6zn2 Chain E (length=335) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQ
YRHGDPIPRVEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFS
GYREDNIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQ
YIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEE
IEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHCLSEEPEIRAF
DPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPY
TLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIG
Ligand information
Ligand IDFE
InChIInChI=1S/Fe/q+3
InChIKeyVTLYFUHAOXGGBS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[Fe+3]
FormulaFe
NameFE (III) ION
ChEMBL
DrugBankDB13949
ZINC
PDB chain6zn2 Chain E Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6zn2 Structural mechanism for tyrosine hydroxylase inhibition by dopamine and reactivation by Ser40 phosphorylation.
Resolution4.3 Å
Binding residue
(original residue number in PDB)
H330 H335 E375
Binding residue
(residue number reindexed from 1)
H168 H173 E213
Annotation score1
Enzymatic activity
Enzyme Commision number 1.14.16.2: tyrosine 3-monooxygenase.
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016714 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen
Biological Process
GO:0009072 aromatic amino acid metabolic process

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Molecular Function

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Biological Process
External links
PDB RCSB:6zn2, PDBe:6zn2, PDBj:6zn2
PDBsum6zn2
PubMed35013193
UniProtP07101|TY3H_HUMAN Tyrosine 3-monooxygenase (Gene Name=TH)

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